T2DP4_PIRLC
ID T2DP4_PIRLC Reviewed; 37 AA.
AC P83259;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Delta-amaurobitoxin-Pl1d {ECO:0000305};
DE Short=Delta-AMATX-Pl1d {ECO:0000305};
DE AltName: Full=Delta-palutoxin IT4 {ECO:0000303|PubMed:10971590};
DE Short=Delta-paluIT4 {ECO:0000303|PubMed:10971590};
OS Pireneitega luctuosa (Tangled nest spider) (Paracoelotes luctuosus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC Araneomorphae; Entelegynae; Agelenidae; Pireneitega.
OX NCBI_TaxID=185217;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, AMIDATION AT SER-37, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=10971590; DOI=10.1046/j.1432-1327.2000.01653.x;
RA Corzo G., Escoubas P., Stankiewicz M., Pelhate M., Kristensen C.P.,
RA Nakajima T.;
RT "Isolation, synthesis and pharmacological characterization of delta-
RT palutoxins IT, novel insecticidal toxins from the spider Paracoelotes
RT luctuosus (Amaurobiidae).";
RL Eur. J. Biochem. 267:5783-5795(2000).
CC -!- FUNCTION: Binds at site 4 of sodium channels (Nav) and inhibits the
CC fast inactivation of cockroach channels. This toxin is active only on
CC insects (By similarity) Has a potent activity against S.litura larvae.
CC {ECO:0000250, ECO:0000269|PubMed:10971590}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:10971590}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin. {ECO:0000250}.
CC -!- MASS SPECTROMETRY: Mass=4052.3; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10971590};
CC -!- SIMILARITY: Belongs to the neurotoxin 07 (Beta/delta-agtx) family. 01
CC (aga-2) subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P83259; -.
DR SMR; P83259; -.
DR ArachnoServer; AS000304; delta-Amaurobitoxin-Pl1d.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0017080; F:sodium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR GO; GO:0035821; P:modulation of process of another organism; IDA:UniProtKB.
DR InterPro; IPR016328; Beta/delta-agatoxin_fam.
DR PIRSF; PIRSF001882; Curtatoxin; 1.
DR PROSITE; PS60015; MU_AGATOXIN; 1.
PE 1: Evidence at protein level;
KW Amidation; Direct protein sequencing; Disulfide bond;
KW Ion channel impairing toxin; Knottin; Neurotoxin; Secreted; Toxin;
KW Voltage-gated sodium channel impairing toxin.
FT PEPTIDE 1..37
FT /note="Delta-amaurobitoxin-Pl1d"
FT /evidence="ECO:0000269|PubMed:10971590"
FT /id="PRO_0000044964"
FT SITE 8
FT /note="Pharmacophore"
FT /evidence="ECO:0000250"
FT SITE 12
FT /note="Pharmacophore"
FT /evidence="ECO:0000250"
FT SITE 22
FT /note="Pharmacophore"
FT /evidence="ECO:0000250"
FT SITE 24
FT /note="Pharmacophore"
FT /evidence="ECO:0000250"
FT SITE 26
FT /note="Pharmacophore"
FT /evidence="ECO:0000250"
FT SITE 34
FT /note="Pharmacophore"
FT /evidence="ECO:0000250"
FT MOD_RES 37
FT /note="Serine amide"
FT /evidence="ECO:0000269|PubMed:10971590"
FT DISULFID 2..18
FT /evidence="ECO:0000250|UniProtKB:P83257"
FT DISULFID 9..23
FT /evidence="ECO:0000250|UniProtKB:P83257"
FT DISULFID 17..33
FT /evidence="ECO:0000250|UniProtKB:P83257"
FT DISULFID 25..31
FT /evidence="ECO:0000250|UniProtKB:P83257"
SQ SEQUENCE 37 AA; 4062 MW; 7F9C5516D556E70C CRC64;
ACATKNQRCA SWAGPYCCDG FYCSCRSYPG CMCRPNS
